Collagen found in the subendothelium is thought to be one of the first thrombogenic stimuli presented to blood at the site of a damaged or diseased vessel wall. In vitro collagen promotes both platelet adhesion and aggregation and subsequent activation of platelets.
Echistatin and its ability to inhibit platelet aggregation by binding to the fibrinogen receptor glycoprotein IIb/IIIa is described in Gan et al. (1988) J. Biol. Chem. 263, pp. 19827-19832; Garsky et al. (1989) Proc. Natl. Acad. Sic. USA 86, pp. 4022-4026; and Gan et al. (1989) Gene 79, 159-166.
Simonidesz et al., U.S. Pat. No. 4,520,018, describes 5-substituted-4-oxo PGI1 derivatives which inhibit blood platelet aggregation induced by ADP, arachidic acid, or collagen and improve blood circulation.
Coan, U.S. Pat. No. 4,229,540, describes a hydrolytic enzyme found in human plasma which inhibits plate let aggregation induced by ADP, epinephrine or collagen.
Rouslahti et al., U.S. Pat. No. 4,578,079, describes the primary cell-binding site of fibronectin as a short amino acid sequence, Arg-Gly-Asp-Ser, that is shared by at least one other adhesive protein, collagen.